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P20618

- PSB1_HUMAN

UniProt

P20618 - PSB1_HUMAN

Protein

Proteasome subunit beta type-1

Gene

PSMB1

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 160 (01 Oct 2014)
      Sequence version 2 (01 May 1992)
      Previous versions | rss
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    Functioni

    The proteasome is a multicatalytic proteinase complex which is characterized by its ability to cleave peptides with Arg, Phe, Tyr, Leu, and Glu adjacent to the leaving group at neutral or slightly basic pH. The proteasome has an ATP-dependent proteolytic activity.

    Catalytic activityi

    Cleavage of peptide bonds with very broad specificity.

    GO - Molecular functioni

    1. protein binding Source: IntAct
    2. threonine-type endopeptidase activity Source: UniProtKB-KW

    GO - Biological processi

    1. anaphase-promoting complex-dependent proteasomal ubiquitin-dependent protein catabolic process Source: Reactome
    2. antigen processing and presentation of exogenous peptide antigen via MHC class I Source: Reactome
    3. antigen processing and presentation of exogenous peptide antigen via MHC class I, TAP-dependent Source: Reactome
    4. antigen processing and presentation of peptide antigen via MHC class I Source: Reactome
    5. apoptotic process Source: Reactome
    6. cellular nitrogen compound metabolic process Source: Reactome
    7. DNA damage response, signal transduction by p53 class mediator resulting in cell cycle arrest Source: Reactome
    8. G1/S transition of mitotic cell cycle Source: Reactome
    9. gene expression Source: Reactome
    10. mitotic cell cycle Source: Reactome
    11. mRNA metabolic process Source: Reactome
    12. negative regulation of apoptotic process Source: Reactome
    13. negative regulation of ubiquitin-protein ligase activity involved in mitotic cell cycle Source: Reactome
    14. positive regulation of ubiquitin-protein ligase activity involved in mitotic cell cycle Source: Reactome
    15. protein polyubiquitination Source: Reactome
    16. regulation of apoptotic process Source: Reactome
    17. regulation of cellular amino acid metabolic process Source: Reactome
    18. regulation of ubiquitin-protein ligase activity involved in mitotic cell cycle Source: Reactome
    19. RNA metabolic process Source: Reactome
    20. small molecule metabolic process Source: Reactome
    21. viral process Source: Reactome

    Keywords - Molecular functioni

    Hydrolase, Protease, Threonine protease

    Keywords - Biological processi

    Host-virus interaction

    Enzyme and pathway databases

    ReactomeiREACT_111056. Cross-presentation of soluble exogenous antigens (endosomes).
    REACT_111178. ER-Phagosome pathway.
    REACT_1156. Orc1 removal from chromatin.
    REACT_118656. Activation of NF-kappaB in B cells.
    REACT_1221. CDK-mediated phosphorylation and removal of Cdc6.
    REACT_13464. Regulation of activated PAK-2p34 by proteasome mediated degradation.
    REACT_13565. Regulation of ornithine decarboxylase (ODC).
    REACT_150471. Separation of Sister Chromatids.
    REACT_1614. Ubiquitin Mediated Degradation of Phosphorylated Cdc25A.
    REACT_172638. Asymmetric localization of PCP proteins.
    REACT_1949. CDT1 association with the CDC6:ORC:origin complex.
    REACT_200766. degradation of AXIN.
    REACT_200841. degradation of DVL.
    REACT_20549. Autodegradation of the E3 ubiquitin ligase COP1.
    REACT_25325. AUF1 (hnRNP D0) destabilizes mRNA.
    REACT_4. Ubiquitin-dependent degradation of Cyclin D1.
    REACT_6761. APC/C:Cdh1 mediated degradation of Cdc20 and other APC/C:Cdh1 targeted proteins in late mitosis/early G1.
    REACT_6785. Autodegradation of Cdh1 by Cdh1:APC/C.
    REACT_6821. SCF-beta-TrCP mediated degradation of Emi1.
    REACT_6871. APC/C:Cdc20 mediated degradation of Securin.
    REACT_75842. Antigen processing: Ubiquitination & Proteasome degradation.
    REACT_9003. SCF(Skp2)-mediated degradation of p27/p21.
    REACT_9031. Vpu mediated degradation of CD4.
    REACT_9453. Vif-mediated degradation of APOBEC3G.

    Protein family/group databases

    MEROPSiT01.986.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Proteasome subunit beta type-1 (EC:3.4.25.1)
    Alternative name(s):
    Macropain subunit C5
    Multicatalytic endopeptidase complex subunit C5
    Proteasome component C5
    Proteasome gamma chain
    Gene namesi
    Name:PSMB1
    Synonyms:PSC5
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 6

    Organism-specific databases

    HGNCiHGNC:9537. PSMB1.

    Subcellular locationi

    GO - Cellular componenti

    1. cytosol Source: Reactome
    2. extracellular vesicular exosome Source: UniProt
    3. nucleoplasm Source: Reactome
    4. nucleus Source: UniProt
    5. proteasome complex Source: ProtInc
    6. proteasome core complex Source: UniProtKB

    Keywords - Cellular componenti

    Cytoplasm, Nucleus, Proteasome

    Pathology & Biotechi

    Organism-specific databases

    PharmGKBiPA33882.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Propeptidei1 – 28281 PublicationPRO_0000259623Add
    BLAST
    Chaini29 – 241213Proteasome subunit beta type-1PRO_0000148030Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei1 – 11N-acetylmethionine1 Publication
    Glycosylationi58 – 581O-linked (GlcNAc)By similarity
    Modified residuei150 – 1501PhosphotyrosineBy similarity
    Modified residuei204 – 2041N6-acetyllysine1 Publication
    Glycosylationi209 – 2091O-linked (GlcNAc)By similarity

    Keywords - PTMi

    Acetylation, Glycoprotein, Phosphoprotein

    Proteomic databases

    MaxQBiP20618.
    PaxDbiP20618.
    PeptideAtlasiP20618.
    PRIDEiP20618.

    2D gel databases

    REPRODUCTION-2DPAGEIPI00025019.
    UCD-2DPAGEP20618.

    PTM databases

    PhosphoSiteiP20618.

    Expressioni

    Gene expression databases

    BgeeiP20618.
    CleanExiHS_PSMB1.
    GenevestigatoriP20618.

    Organism-specific databases

    HPAiCAB033911.
    HPA029635.
    HPA029637.

    Interactioni

    Subunit structurei

    The 26S proteasome consists of a 20S proteasome core and two 19S regulatory subunits. The 20S proteasome core is composed of 28 subunits that are arranged in four stacked rings, resulting in a barrel-shaped structure. The two end rings are each formed by seven alpha subunits, and the two central rings are each formed by seven beta subunits. The catalytic chamber with the active sites is on the inside of the barrel. Interacts with SERPINB2. Interacts with HIV-1 TAT protein.2 Publications

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    PSMB5P280743EBI-372273,EBI-357828
    PSMB7Q994368EBI-372273,EBI-603319

    Protein-protein interaction databases

    BioGridi111662. 99 interactions.
    IntActiP20618. 21 interactions.
    MINTiMINT-3009312.
    STRINGi9606.ENSP00000262193.

    Structurei

    3D structure databases

    ProteinModelPortaliP20618.
    SMRiP20618. Positions 29-241.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Sequence similaritiesi

    Belongs to the peptidase T1B family.PROSITE-ProRule annotation

    Phylogenomic databases

    eggNOGiCOG0638.
    HOGENOMiHOG000091081.
    HOVERGENiHBG000961.
    InParanoidiP20618.
    KOiK02732.
    OMAiNAPEPEM.
    OrthoDBiEOG7WHHBB.
    PhylomeDBiP20618.
    TreeFamiTF106218.

    Family and domain databases

    Gene3Di3.60.20.10. 1 hit.
    InterProiIPR029055. Ntn_hydrolases_N.
    IPR016050. Proteasome_bsu_CS.
    IPR001353. Proteasome_sua/b.
    IPR023333. Proteasome_suB-type.
    [Graphical view]
    PfamiPF00227. Proteasome. 1 hit.
    [Graphical view]
    SUPFAMiSSF56235. SSF56235. 1 hit.
    PROSITEiPS00854. PROTEASOME_BETA_1. 1 hit.
    PS51476. PROTEASOME_BETA_2. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    Sequence processingi: The displayed sequence is further processed into a mature form.

    P20618-1 [UniParc]FASTAAdd to Basket

    « Hide

    MLSSTAMYSA PGRDLGMEPH RAAGPLQLRF SPYVFNGGTI LAIAGEDFAI    50
    VASDTRLSEG FSIHTRDSPK CYKLTDKTVI GCSGFHGDCL TLTKIIEARL 100
    KMYKHSNNKA MTTGAIAAML STILYSRRFF PYYVYNIIGG LDEEGKGAVY 150
    SFDPVGSYQR DSFKAGGSAS AMLQPLLDNQ VGFKNMQNVE HVPLSLDRAM 200
    RLVKDVFISA AERDVYTGDA LRICIVTKEG IREETVSLRK D 241
    Length:241
    Mass (Da):26,489
    Last modified:May 1, 1992 - v2
    Checksum:iAE8FC42799F39157
    GO

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti11 – 111P → A.1 Publication
    Corresponds to variant rs12717 [ dbSNP | Ensembl ].
    VAR_051547
    Natural varianti208 – 2081I → N.
    Corresponds to variant rs10541 [ dbSNP | Ensembl ].
    VAR_051548

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    D00761 mRNA. Translation: BAA00658.1.
    BT019720 mRNA. Translation: AAV38525.1.
    AB451312 mRNA. Translation: BAG70126.1.
    AB451442 mRNA. Translation: BAG70256.1.
    AL031259 Genomic DNA. Translation: CAA20287.1.
    BC000508 mRNA. Translation: AAH00508.1.
    BC020807 mRNA. Translation: AAH20807.1.
    CCDSiCCDS34577.1.
    PIRiS15973. SNHUC5.
    RefSeqiNP_002784.1. NM_002793.3.
    UniGeneiHs.352768.

    Genome annotation databases

    EnsembliENST00000262193; ENSP00000262193; ENSG00000008018.
    GeneIDi5689.
    KEGGihsa:5689.
    UCSCiuc003qxr.3. human.

    Polymorphism databases

    DMDMi130853.

    Keywords - Coding sequence diversityi

    Polymorphism

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    D00761 mRNA. Translation: BAA00658.1 .
    BT019720 mRNA. Translation: AAV38525.1 .
    AB451312 mRNA. Translation: BAG70126.1 .
    AB451442 mRNA. Translation: BAG70256.1 .
    AL031259 Genomic DNA. Translation: CAA20287.1 .
    BC000508 mRNA. Translation: AAH00508.1 .
    BC020807 mRNA. Translation: AAH20807.1 .
    CCDSi CCDS34577.1.
    PIRi S15973. SNHUC5.
    RefSeqi NP_002784.1. NM_002793.3.
    UniGenei Hs.352768.

    3D structure databases

    ProteinModelPortali P20618.
    SMRi P20618. Positions 29-241.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 111662. 99 interactions.
    IntActi P20618. 21 interactions.
    MINTi MINT-3009312.
    STRINGi 9606.ENSP00000262193.

    Chemistry

    BindingDBi P20618.
    ChEMBLi CHEMBL2364701.
    DrugBanki DB00188. Bortezomib.

    Protein family/group databases

    MEROPSi T01.986.

    PTM databases

    PhosphoSitei P20618.

    Polymorphism databases

    DMDMi 130853.

    2D gel databases

    REPRODUCTION-2DPAGE IPI00025019.
    UCD-2DPAGE P20618.

    Proteomic databases

    MaxQBi P20618.
    PaxDbi P20618.
    PeptideAtlasi P20618.
    PRIDEi P20618.

    Protocols and materials databases

    DNASUi 5689.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000262193 ; ENSP00000262193 ; ENSG00000008018 .
    GeneIDi 5689.
    KEGGi hsa:5689.
    UCSCi uc003qxr.3. human.

    Organism-specific databases

    CTDi 5689.
    GeneCardsi GC06M170844.
    HGNCi HGNC:9537. PSMB1.
    HPAi CAB033911.
    HPA029635.
    HPA029637.
    MIMi 602017. gene.
    neXtProti NX_P20618.
    PharmGKBi PA33882.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi COG0638.
    HOGENOMi HOG000091081.
    HOVERGENi HBG000961.
    InParanoidi P20618.
    KOi K02732.
    OMAi NAPEPEM.
    OrthoDBi EOG7WHHBB.
    PhylomeDBi P20618.
    TreeFami TF106218.

    Enzyme and pathway databases

    Reactomei REACT_111056. Cross-presentation of soluble exogenous antigens (endosomes).
    REACT_111178. ER-Phagosome pathway.
    REACT_1156. Orc1 removal from chromatin.
    REACT_118656. Activation of NF-kappaB in B cells.
    REACT_1221. CDK-mediated phosphorylation and removal of Cdc6.
    REACT_13464. Regulation of activated PAK-2p34 by proteasome mediated degradation.
    REACT_13565. Regulation of ornithine decarboxylase (ODC).
    REACT_150471. Separation of Sister Chromatids.
    REACT_1614. Ubiquitin Mediated Degradation of Phosphorylated Cdc25A.
    REACT_172638. Asymmetric localization of PCP proteins.
    REACT_1949. CDT1 association with the CDC6:ORC:origin complex.
    REACT_200766. degradation of AXIN.
    REACT_200841. degradation of DVL.
    REACT_20549. Autodegradation of the E3 ubiquitin ligase COP1.
    REACT_25325. AUF1 (hnRNP D0) destabilizes mRNA.
    REACT_4. Ubiquitin-dependent degradation of Cyclin D1.
    REACT_6761. APC/C:Cdh1 mediated degradation of Cdc20 and other APC/C:Cdh1 targeted proteins in late mitosis/early G1.
    REACT_6785. Autodegradation of Cdh1 by Cdh1:APC/C.
    REACT_6821. SCF-beta-TrCP mediated degradation of Emi1.
    REACT_6871. APC/C:Cdc20 mediated degradation of Securin.
    REACT_75842. Antigen processing: Ubiquitination & Proteasome degradation.
    REACT_9003. SCF(Skp2)-mediated degradation of p27/p21.
    REACT_9031. Vpu mediated degradation of CD4.
    REACT_9453. Vif-mediated degradation of APOBEC3G.

    Miscellaneous databases

    ChiTaRSi PSMB1. human.
    GeneWikii PSMB1.
    GenomeRNAii 5689.
    NextBioi 22098.
    PROi P20618.
    SOURCEi Search...

    Gene expression databases

    Bgeei P20618.
    CleanExi HS_PSMB1.
    Genevestigatori P20618.

    Family and domain databases

    Gene3Di 3.60.20.10. 1 hit.
    InterProi IPR029055. Ntn_hydrolases_N.
    IPR016050. Proteasome_bsu_CS.
    IPR001353. Proteasome_sua/b.
    IPR023333. Proteasome_suB-type.
    [Graphical view ]
    Pfami PF00227. Proteasome. 1 hit.
    [Graphical view ]
    SUPFAMi SSF56235. SSF56235. 1 hit.
    PROSITEi PS00854. PROTEASOME_BETA_1. 1 hit.
    PS51476. PROTEASOME_BETA_2. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Molecular cloning and sequence analysis of cDNAs for five major subunits of human proteasomes (multi-catalytic proteinase complexes)."
      Tamura T., Lee D.H., Osaka F., Fujiwara T., Shin S., Chung C.H., Tanaka K., Ichihara A.
      Biochim. Biophys. Acta 1089:95-102(1991) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    2. "Cloning of human full-length CDSs in BD Creator(TM) system donor vector."
      Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S., Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y., Phelan M., Farmer A.
      Submitted (OCT-2004) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    3. "Human protein factory for converting the transcriptome into an in vitro-expressed proteome."
      Goshima N., Kawamura Y., Fukumoto A., Miura A., Honma R., Satoh R., Wakamatsu A., Yamamoto J., Kimura K., Nishikawa T., Andoh T., Iida Y., Ishikawa K., Ito E., Kagawa N., Kaminaga C., Kanehori K., Kawakami B.
      , Kenmochi K., Kimura R., Kobayashi M., Kuroita T., Kuwayama H., Maruyama Y., Matsuo K., Minami K., Mitsubori M., Mori M., Morishita R., Murase A., Nishikawa A., Nishikawa S., Okamoto T., Sakagami N., Sakamoto Y., Sasaki Y., Seki T., Sono S., Sugiyama A., Sumiya T., Takayama T., Takayama Y., Takeda H., Togashi T., Yahata K., Yamada H., Yanagisawa Y., Endo Y., Imamoto F., Kisu Y., Tanaka S., Isogai T., Imai J., Watanabe S., Nomura N.
      Nat. Methods 5:1011-1017(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    4. "The DNA sequence and analysis of human chromosome 6."
      Mungall A.J., Palmer S.A., Sims S.K., Edwards C.A., Ashurst J.L., Wilming L., Jones M.C., Horton R., Hunt S.E., Scott C.E., Gilbert J.G.R., Clamp M.E., Bethel G., Milne S., Ainscough R., Almeida J.P., Ambrose K.D., Andrews T.D.
      , Ashwell R.I.S., Babbage A.K., Bagguley C.L., Bailey J., Banerjee R., Barker D.J., Barlow K.F., Bates K., Beare D.M., Beasley H., Beasley O., Bird C.P., Blakey S.E., Bray-Allen S., Brook J., Brown A.J., Brown J.Y., Burford D.C., Burrill W., Burton J., Carder C., Carter N.P., Chapman J.C., Clark S.Y., Clark G., Clee C.M., Clegg S., Cobley V., Collier R.E., Collins J.E., Colman L.K., Corby N.R., Coville G.J., Culley K.M., Dhami P., Davies J., Dunn M., Earthrowl M.E., Ellington A.E., Evans K.A., Faulkner L., Francis M.D., Frankish A., Frankland J., French L., Garner P., Garnett J., Ghori M.J., Gilby L.M., Gillson C.J., Glithero R.J., Grafham D.V., Grant M., Gribble S., Griffiths C., Griffiths M.N.D., Hall R., Halls K.S., Hammond S., Harley J.L., Hart E.A., Heath P.D., Heathcott R., Holmes S.J., Howden P.J., Howe K.L., Howell G.R., Huckle E., Humphray S.J., Humphries M.D., Hunt A.R., Johnson C.M., Joy A.A., Kay M., Keenan S.J., Kimberley A.M., King A., Laird G.K., Langford C., Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C.R., Lloyd D.M., Loveland J.E., Lovell J., Martin S., Mashreghi-Mohammadi M., Maslen G.L., Matthews L., McCann O.T., McLaren S.J., McLay K., McMurray A., Moore M.J.F., Mullikin J.C., Niblett D., Nickerson T., Novik K.L., Oliver K., Overton-Larty E.K., Parker A., Patel R., Pearce A.V., Peck A.I., Phillimore B.J.C.T., Phillips S., Plumb R.W., Porter K.M., Ramsey Y., Ranby S.A., Rice C.M., Ross M.T., Searle S.M., Sehra H.K., Sheridan E., Skuce C.D., Smith S., Smith M., Spraggon L., Squares S.L., Steward C.A., Sycamore N., Tamlyn-Hall G., Tester J., Theaker A.J., Thomas D.W., Thorpe A., Tracey A., Tromans A., Tubby B., Wall M., Wallis J.M., West A.P., White S.S., Whitehead S.L., Whittaker H., Wild A., Willey D.J., Wilmer T.E., Wood J.M., Wray P.W., Wyatt J.C., Young L., Younger R.M., Bentley D.R., Coulson A., Durbin R.M., Hubbard T., Sulston J.E., Dunham I., Rogers J., Beck S.
      Nature 425:805-811(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    5. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
      The MGC Project Team
      Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], VARIANT ALA-11.
      Tissue: Brain and Lung.
    6. "Relationships among the subunits of the high molecular weight proteinase, macropain (proteasome)."
      Lee L.W., Moomaw C.R., Orth K., McGuire M.J., DeMartino G.N., Slaughter C.A.
      Biochim. Biophys. Acta 1037:178-185(1990) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE OF 29-52.
    7. "Human immunodeficiency virus-1 Tat protein interacts with distinct proteasomal alpha and beta subunits."
      Apcher G.S., Heink S., Zantopf D., Kloetzel P.-M., Schmid H.-P., Mayer R.J., Krueger E.
      FEBS Lett. 553:200-204(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH HIV-1 TAT.
    8. "Interaction of plasminogen activator inhibitor-2 and proteasome subunit, beta type 1."
      Fan J., Zhang Y.Q., Li P., Hou M., Tan L., Wang X., Zhu Y.S.
      Acta Biochim. Biophys. Sin. 36:42-46(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH SERPINB2.
    9. "Mass spectrometric characterization of the affinity-purified human 26S proteasome complex."
      Wang X., Chen C.-F., Baker P.R., Chen P.-L., Kaiser P., Huang L.
      Biochemistry 46:3553-3565(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Embryonic kidney.
    10. "Lysine acetylation targets protein complexes and co-regulates major cellular functions."
      Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C., Olsen J.V., Mann M.
      Science 325:834-840(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-204, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    11. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    12. Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

    Entry informationi

    Entry nameiPSB1_HUMAN
    AccessioniPrimary (citable) accession number: P20618
    Secondary accession number(s): B5BU76, Q9BWA8
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: February 1, 1991
    Last sequence update: May 1, 1992
    Last modified: October 1, 2014
    This is version 160 of the entry and version 2 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programChordata Protein Annotation Program
    DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

    Miscellaneousi

    Keywords - Technical termi

    Complete proteome, Direct protein sequencing, Reference proteome

    Documents

    1. Human chromosome 6
      Human chromosome 6: entries, gene names and cross-references to MIM
    2. Human entries with polymorphisms or disease mutations
      List of human entries with polymorphisms or disease mutations
    3. Human polymorphisms and disease mutations
      Index of human polymorphisms and disease mutations
    4. MIM cross-references
      Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
    5. Peptidase families
      Classification of peptidase families and list of entries
    6. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3